Mortensson-Egnund K, Schöyen R, Howe C, Lee L T, Harboe A
J Bacteriol. 1969 Jun;98(3):924-9. doi: 10.1128/jb.98.3.924-929.1969.
Intracellular glycosidases were measured in cell-free extracts obtained by ultrasonic disruption of a gram-negative soil coccobacillus (Chase, 1938). From these extracts, alpha-l-fucosidase was purified about 120-fold by salting out with (NH(4))(2)SO(4), ion exchange chromatography, and gel filtration. The approximate molecular weight of the enzyme was 50,000; its pH optimum was 5. The enzyme was inhibited by l-fucose and split this sugar from a purified acid mucopolysaccharide from chicken chorioallantoic fluid. The acid mucopolysaccharide is identical with a component (host antigen) of the hemagglutinin of influenza virus. Its antigenic reactivity is altered by cell-free extracts of the bacterium, in which the responsible enzyme is thought to be an alpha-l-fucosidase.
通过超声破碎革兰氏阴性土壤球杆菌（Chase，1938）获得无细胞提取物，测定其中的细胞内糖苷酶。从这些提取物中，通过硫酸铵盐析、离子交换色谱和凝胶过滤，将α-L-岩藻糖苷酶纯化了约120倍。该酶的近似分子量为50,000；其最适pH为5。该酶被L-岩藻糖抑制，并从鸡绒毛尿囊液的纯化酸性粘多糖中裂解出这种糖。该酸性粘多糖与流感病毒血凝素的一种成分（宿主抗原）相同。其抗原反应性会被该细菌的无细胞提取物改变，其中起作用的酶被认为是一种α-L-岩藻糖苷酶。
